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Carboxypeptidase B2 (EC 3.4.17.20) (Carboxypeptidase R) (CPR) (Carboxypeptidase U) (CPU) (Thrombin-activable fibrinolysis inhibitor) (TAFI)

 CBPB2_RAT               Reviewed;         422 AA.
Q9EQV9; Q3B7V3; Q5BKB8;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 110.
RecName: Full=Carboxypeptidase B2;
EC=3.4.17.20;
AltName: Full=Carboxypeptidase R;
Short=CPR;
AltName: Full=Carboxypeptidase U;
Short=CPU;
AltName: Full=Thrombin-activable fibrinolysis inhibitor;
Short=TAFI;
Flags: Precursor;
Name=Cpb2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=11021404; DOI=10.1111/j.1348-0421.2000.tb02555.x;
Kato T., Sato T., Matsuo S., Yamamoto T., Campbell W., Hotta N.,
Okada N., Okada H.;
"Molecular cloning and partial characterization of rat
procarboxypeptidase R and carboxypeptidase N.";
Microbiol. Immunol. 44:719-728(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Cleaves C-terminal arginine or lysine residues from
biologically active peptides such as kinins or anaphylatoxins in
the circulation thereby regulating their activities. Down-
regulates fibrinolysis by removing C-terminal lysine residues from
fibrin that has already been partially degraded by plasmin.
{ECO:0000269|PubMed:11021404}.
-!- CATALYTIC ACTIVITY: Release of C-terminal Arg and Lys from a
polypeptide.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P00730};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
-!- ENZYME REGULATION: TAFI/CPB2 is unique among carboxypeptidases in
that it spontaneously inactivates with a short half-life, a
property that is crucial for its role in controlling blood clot
lysis. The zymogen is stabilized by interactions with the
activation peptide. Release of the activation peptide increases a
dynamic flap mobility and in time this leads to conformational
changes that disrupt the catalytic site and expose a cryptic
thrombin-cleavage site present at Arg-323 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
-!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB042598; BAB18617.1; -; mRNA.
EMBL; BC091133; AAH91133.1; -; mRNA.
EMBL; BC107447; AAI07448.1; -; mRNA.
RefSeq; NP_446069.1; NM_053617.2.
UniGene; Rn.12572; -.
ProteinModelPortal; Q9EQV9; -.
SMR; Q9EQV9; -.
STRING; 10116.ENSRNOP00000014909; -.
MEROPS; M14.009; -.
PhosphoSitePlus; Q9EQV9; -.
PaxDb; Q9EQV9; -.
PRIDE; Q9EQV9; -.
Ensembl; ENSRNOT00000014909; ENSRNOP00000014909; ENSRNOG00000010935.
GeneID; 113936; -.
KEGG; rno:113936; -.
UCSC; RGD:71035; rat.
CTD; 1361; -.
RGD; 71035; Cpb2.
eggNOG; KOG2650; Eukaryota.
eggNOG; COG2866; LUCA.
GeneTree; ENSGT00760000119103; -.
HOGENOM; HOG000252968; -.
HOVERGEN; HBG050815; -.
InParanoid; Q9EQV9; -.
KO; K01300; -.
OMA; EIYSWIE; -.
OrthoDB; EOG091G0HUI; -.
PhylomeDB; Q9EQV9; -.
TreeFam; TF317197; -.
BRENDA; 3.4.17.20; 5301.
Reactome; R-RNO-977606; Regulation of Complement cascade.
PRO; PR:Q9EQV9; -.
Proteomes; UP000002494; Chromosome 15.
Bgee; ENSRNOG00000010935; -.
Genevisible; Q9EQV9; RN.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0004180; F:carboxypeptidase activity; IDA:RGD.
GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0042730; P:fibrinolysis; IMP:RGD.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:RGD.
GO; GO:2000346; P:negative regulation of hepatocyte proliferation; IMP:RGD.
GO; GO:0010757; P:negative regulation of plasminogen activation; IMP:RGD.
GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; IMP:RGD.
GO; GO:0006508; P:proteolysis; IDA:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0009408; P:response to heat; IDA:RGD.
CDD; cd06246; M14_CPB2; 1.
Gene3D; 3.30.70.340; -; 1.
InterPro; IPR033849; CPB2.
InterPro; IPR036990; M14A-like_propep.
InterPro; IPR003146; M14A_act_pep.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000834; Peptidase_M14.
Pfam; PF00246; Peptidase_M14; 1.
Pfam; PF02244; Propep_M14; 1.
PRINTS; PR00765; CRBOXYPTASEA.
SMART; SM00631; Zn_pept; 1.
SUPFAM; SSF54897; SSF54897; 1.
2: Evidence at transcript level;
Blood coagulation; Carboxypeptidase; Complete proteome;
Disulfide bond; Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase;
Metal-binding; Metalloprotease; Protease; Reference proteome;
Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 113 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000004381.
CHAIN 114 422 Carboxypeptidase B2.
/FTId=PRO_0000004382.
REGION 180 183 Substrate binding.
{ECO:0000250|UniProtKB:P00730}.
REGION 255 256 Substrate binding.
{ECO:0000250|UniProtKB:P00730}.
REGION 310 311 Substrate binding.
{ECO:0000250|UniProtKB:P00730}.
ACT_SITE 384 384 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P00732}.
METAL 180 180 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
METAL 183 183 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
METAL 309 309 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
BINDING 238 238 Substrate.
{ECO:0000250|UniProtKB:P00730}.
BINDING 362 362 Substrate.
{ECO:0000250|UniProtKB:P00730}.
SITE 323 324 Cleavage; by thrombin. {ECO:0000250}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 177 190 {ECO:0000250|UniProtKB:Q96IY4}.
DISULFID 249 273 {ECO:0000250|UniProtKB:Q96IY4}.
DISULFID 264 278 {ECO:0000250|UniProtKB:Q96IY4}.
SEQUENCE 422 AA; 48827 MW; FFFD32A51A9366C8 CRC64;
MKLYGLGVLV AIILYEKHGL AFQSGHVLSA LPRTSRQVQL LQNLTTTYEV VLWQPVTAEF
IEKKKEVHFF VNASDVNSVK AYLNASRIPF NVLMNNVEDL IQQQTSNDTV SPRASSSYYE
QYHSLNEIYS WIEVITEQHP DMLQKIYIGS SYEKYPLYVL KVSGKEHRVK NAIWIDCGIH
AREWISPAFC LWFIGYVTQF HGKENTYTRL LRHVDFYIMP VMNVDGYDYT WKKNRMWRKN
RSVHMNNRCV GTDLNRNFAS KHWCEKGASS FSCSETYCGL YPESEPEVKA VADFLRRNIN
HIKAYISMHS YSQQILFPYS YNRSKSKDHE ELSLVASEAV RAIESINKNT RYTHGSGSES
LYLAPGGSDD WIYDLGIKYS FTIELRDTGR YGFLLPERFI KPTCAEALAA VSKIAWHVIR
NS


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